Scribd
Upload
65 views31 pages

Enzyme Kinetics and Inhibition Explained

This lecture discusses enzyme kinetics and inhibition. It introduces Michaelis-Menten kinetics to describe the rate of enzymatic reactions and defines key terms like KM, Vmax, and turnover number. It then examines different types of enzyme inhibition, including competitive inhibition where an inhibitor competes with the substrate for binding site, uncompetitive inhibition where the inhibitor only binds the enzyme-substrate complex, and noncompetitive inhibition where the inhibitor can bind the free enzyme or enzyme-substrate complex. Lineweaver-Burk plots are used to analyze the effects of each type of inhibition on the Michaelis-Menten kinetics.

Uploaded by

Shyam Dave
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
65 views31 pages

Enzyme Kinetics and Inhibition Explained

This lecture discusses enzyme kinetics and inhibition. It introduces Michaelis-Menten kinetics to describe the rate of enzymatic reactions and defines key terms like KM, Vmax, and turnover number. It then examines different types of enzyme inhibition, including competitive inhibition where an inhibitor competes with the substrate for binding site, uncompetitive inhibition where the inhibitor only binds the enzyme-substrate complex, and noncompetitive inhibition where the inhibitor can bind the free enzyme or enzyme-substrate complex. Lineweaver-Burk plots are used to analyze the effects of each type of inhibition on the Michaelis-Menten kinetics.

Uploaded by

Shyam Dave
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd

Lecture 15

Chemical Reaction Engineering (CRE) is the


field that studies the rates and mechanisms of
chemical reactions and the design of the reactors in
which they take place.
Today’s lecture
  Enzymes
  Michealis-Menten Kinetics
  Lineweaver-Burk Plot
  Enzyme Inhibition
  Competitive
  Uncompetitive

2
Last lecture

3
Last lecture

4
Enzymes
Michaelis-Menten Kinetics.
Enzymes are protein like substances with catalytic properties.

Enzyme unease. [From Biochemistry, 3/E by Stryer, copywrited 1988 by Lubert


Stryer. Used with permission of W.H. Freeman and Company.]

5
Enzymes
It provides a pathway for the substrate to proceed at a faster
rate. The substrate, S, reacts to form a product P.

S Slow P

Fast

A given enzyme can only catalyze only one reaction.


Example, Urea is decomposed by the enzyme urease.
6
7
8
A given enzyme can only catalyze only one reaction. Urea is
decomposed by the enzyme urease, as shown below.

9
The corresponding mechanism is:

10
Michaelis-Menten Kinetics

11
Michaelis-Menten Kinetics

12
Vmax=kcat* Et
Turnover Number: kcat
Number of substrate molecules (moles) converted to product
in a given time (s) on a single enzyme molecule

(molecules/molecule/time)
For the reaction
kcat
H2O2 + E →H2O + O + E

40,000,000 molecules of H2O2 converted to product per second


on a single enzyme molecule.
13
Summary

14
Michaelis-Menten Equation

(Michaelis-Menten plot)
Vmax

-rs Solving:
KM=S1/2
therefore KM is the
S1/2 CS concentration at which the
15 rate is half the maximum rate
Inverting yields

Lineweaver-Burk Plot

1/-rS
slope = KM/Vmax

1/Vmax
16
1/S
Types of Enzyme Inhibition
Competitive

Uncompetitive

Non-competitive

17
Competitive Inhibition

18
Competitive Inhibition

1) Mechanisms:

19
Competitive Inhibition
2) Rates:

20
Competitive Inhibition

21
Competitive Inhibition
From before (no competition):
Increasing CI
Competitive

No Inhibition Competitive

Intercept does not change, slope increases


22
as inhibitor concentration increases
23
Uncompetitive Inhibition
Inhibition only has affinity for enzyme-substrate complex

Developing the rate law

(1)
(2)
24
Adding (1) and (2)

From (2)

25
Total enzyme

26
1 1 ⎛ ⎛ ( I ) ⎞⎞
= ⎜K M + ( S )⎜1+ ⎟⎟
−rS Vmax ( S ) ⎝ ⎝ K I ⎠⎠
1 K M ⎛ 1 ⎞ 1 ⎛ ( I ) ⎞
= ⎜ ⎟ + ⎜1+ ⎟
−rS Vmax ⎝ ( S ) ⎠ Vmax ⎝ K I ⎠

Slope remains the same but intercept changes as inhibitor


concentration
€ is increased

27
Lineweaver-Burk Plot for uncompetitive inhibition
28
Noncompetitive Inhibition (Mixed)
E+S E·S P+E

+I -I -I +I
(inactive)I.E + S I.E.S (inactive)
Increasing I

No Inhibition

Both slope and


intercept changes

29
30
End of Lecture 15

31

You might also like